RECA_BURCE
ID RECA_BURCE Reviewed; 347 AA.
AC P0C7V2; P19690; P77821; Q93LP3;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
OS Burkholderia cepacia (Pseudomonas cepacia).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JN25;
RX PubMed=2227456; DOI=10.1016/0378-1119(90)90471-3;
RA Nakazawa T., Kimoto M., Abe M.;
RT "Cloning, sequencing, and transcriptional analysis of the recA gene of
RT Pseudomonas cepacia.";
RL Gene 94:83-88(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=G4;
RX PubMed=11722883; DOI=10.1128/aem.67.12.5384-5391.2001;
RA Yeager C.M., Bottomley P.J., Arp D.J.;
RT "Requirement of DNA repair mechanisms for survival of Burkholderia cepacia
RT G4 upon degradation of trichloroethylene.";
RL Appl. Environ. Microbiol. 67:5384-5391(2001).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage. {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; D90120; BAA14148.1; -; Genomic_DNA.
DR EMBL; AY036066; AAK64608.1; -; Genomic_DNA.
DR PIR; JQ0459; RQPSAC.
DR AlphaFoldDB; P0C7V2; -.
DR SMR; P0C7V2; -.
DR STRING; 292.DM42_2420; -.
DR eggNOG; COG0468; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; SOS response.
FT CHAIN 1..347
FT /note="Protein RecA"
FT /id="PRO_0000122673"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 32..34
FT /note="EAA -> DVK (in Ref. 2; AAK64608)"
FT /evidence="ECO:0000305"
FT CONFLICT 336..338
FT /note="AGN -> VVD (in Ref. 2; AAK64608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 347 AA; 37258 MW; F3F8B6855CE63BEC CRC64;
MTAEKSKALA AALAQIEKQF GKGSIMRMGD GEAAEDIQVV STGSLGLDIA LGVGGLPRGR
VVEIYGPESS GKTTLTLQVI AELQKLGGTA AFIDAEHALD VQYAAKLGVN VPELLISQPD
TGEQALEITD ALVRSGSIDM IVIDSVAALV PKAEIEGEMG DSLPGLQARL MSQALRKLTG
TIKRTNCLVI FINQIRMKIG VMFGNPETTT GGNALKFYSS VRLDIRRIGS IKKNDEVIGN
ETRVKVVKNK VSPPFREAIF DILYGEGISR QGEIIDLGVQ AKIVDKAGAW YSYNGEKIGQ
GKDNAREFLR ENPEIAREIE NRIRESLGVV AMPDGAGNEA EAMDEEE